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Biomedical subjects

J Jarosz

Publications and source records attributed to J Jarosz.

33 records · Page 2Linked to original sources
PubMed1988

The use of saline W, a physiological salt solution for experimentation on insect immunity.

In a series of induction experiments using various Ringer solutions attempts were made to determine whether saline W, a physiological salt solution for Lepidoptera, when injected into the larval haemocoel of the greater wax moth could be recognized by the insect as a non-self molecule. Laboratory bioassays indicated the loss of insect body integrity following intracoelomic injection of saline W and three other salines, increased levels of haemolymph lysozyme activity (EC 3. 2. 1. 17), and elevated resistance to the bacterial parasite, Pseudomonas aeruginosa. The inducing effect of saline W was stronger than dipterous Ringer's solution or other physiological salines. The stimulating effects indicate that the moth distinguishes between self and non-self, and this provides a new insight into the induction of the immune response.

Animals↗
PubMed1979

Comparative levels of lysozyme activity in larvae and pupae of Galleria mellonella after particulate and soluble materials injection.

Using an assay system for lysozyme activity determination in which haemolymph was compared in activity to known standards, the quantitative shifts in the lysozyme activity level of larvae and pupae of Galleria mellonella, after particulate and soluble materials injection, were compared. The level of this activity in all injected larvae was higher fro that of pupae, but the immune response of pupae was more effective in all treatments when compared with activity in the non-injected controls. Furthermore, there was a significant higher level of lysozyme activity in pupae subjected to mechanical immunizing agents, except inversed pupae in which alternation in activity was not significantly different from activity in the corresponding nonexposed insects. Although the exact role of lysozyme in insect immunity is still uncertain, it is possible that this lysosomal enzyme may degrade the cell wall of susceptible parasites prior to being phagocytosed, and thereby act as a nonspecific inducible humoral defence molecule.

Animals↗
PubMed1978

Polypeptide antibiotic 26a from Bacillus subtilis. I. Taxonomy and fermentative production.

In surface cultures on NK/2-Sym's medium, the isolate No. 26a of Bacillus subtilis from the intestinal tract of Galleria mellonella larvae produced three antibacterial substances which were separated by gel filtration on Sephadex G-25 column. The major bioactive compound named 26a had a close resemblance to bacitracin family of polypeptide antibiotics. Two minor active compounds, i.e. a bacteriolytic enzyme with endo-beta-N-acetylmuramidglycanohydrolase (EC. 3. 2. 1. 17) activity and other unidentified factor were usually synthetized in trace amounts. Maximum yield of 26a generally occurred after 120 hour incubation, when the producer reached the stationary growth phase and general sporulation of the bacterial cultures was found. The basal medium of NK/2-Sym supplemented by addition of manganese ions (10(-4) M), d-glucose (1%) and inorganic nitrogen beneficially resulted in antibiotic potency of the fermentation broth. The antibiotics produced by other isolates (Nos 5AK, 15 and 92) have been also analyzed and from their properties they can be tentatively classified as members of bacitracin group polypeptides. A possible role of the antibiotics produced by intestinal Bacillus spp in the formation process of typical gut microflora of G. mellonella is discussed.

Animals↗
PubMed1978

Polypeptide antibiotic 26a from Bacillus subtilis. II. Isolation and purification procedures.

Both the analytical and preparative methods by which the preparations of 26a bydrochloride salt with a high antibacterial activity and 20--30% recovery have been obtained from the fermentation fluids of Bacillus subtilis are presented. On an industrial scale the antibiotic can be yielded by absorption of bioactivity on Amberlite CG-50I column and precipitation with picric acid of crude substance from active elutes as adduct which was divided on equilibrated CM--cellulose and finally purified by gel filtration on Sephadex G-25 column. The purified preparation gave a single band by SDS-polyacrylamide gel electrophoresis and one ninhydrin-positive spot by thin-layer chromatography on silica gel G plates corresponding to single zones of bioactivity on bioautograms, and moved as a single peak of almost constant antibacterial activity on Sephadex G-75, G-100 and G-200 columns. The potency of the purest preparations, lot Sephadex G-25, was 6,500--7,000 arbitrary units/mg, and were characterized as follows: purification factor, 57; purity of 98--100% by densitometer scans of SDS-polyacrylamide gels; MIC for Sarcina lutea by twofold agar dilution assay, 0.306 microgram/ml.

Animals↗
PubMed1978

Polypeptide antibiotic 26a from Bacillus subtilis. III. Physicochemical and biological in vitro properties.

Antibiotic 26a, a weakly basic (pK1 3.85 and pK2 7.1) polypeptide compound, has been recovered from the fermentation fluids of bacillus subtilis cultures as hydrochloride salt easily soluble in water and dimethylsulphoxide, sparingly soluble in lower alcohols and insoluble in several organic solvents. At low concentrations 26a was effective against gram-positive bacteria, mainly micrococci and corynebacteria, moderately active against mycobacteria, and inactive against gram-negative bacteria, yeasts and moulds even at 300 microgram/ml concentration. From the viewpoint of elemental analysis, electrometric titration, optical rotation, UV, IR and NMR spectra, amino acid composition, molecular weight and biological observations, 26a can be considered as an antibiotic, if not identical, then closely related to bacitracin family polypeptides.

Amino Acids↗
PubMed1978

Polypeptide antibiotic 26a from Bacillus subtilis. IV. Evaluation of biological in vivo activity.

The studies performed with the antibiotic 26a, which has a close resemblance to bacitracin family polypeptide antibiotics, revealed a prominent therapeutic and protective actions. The antibiotic is characterized by a moderately low toxicity, lack of cytotoxic and cytostatic effects on several tissue cultures, and therapeutic effectiveness in lethal streptococcal infections in mice, and corynebacterial infections in guinea pigs.

Animals↗
PubMed1975

[Antibiotic 26a as a factor stimulating the body growth of Japanese quails (Coturnix coturnix japonica)].

Groups I and II of Japanese quails were given 50 ppm of oxytetracyclin and 23 ppm of the antibiotic 26a in drinking water during 3 weeks, from the 7th to the 28th day of life. No antibiotics were given to group III. In order to determine the properties of the antibiotic 26a as a stimulator of growth, the mean values of the body weight gains in the individual groups were compared by statistical methods. During the 1st and 2nd weeks of the experiment, the mean body weight gains in group II were the highest, but in the 3rd week the highest gains were noted in group I. During the whole experiment, the quails in group I had an average gain of 63.18 g, those in group II 66,34 g, and those in group III 63,86 g. Highly significant differences were found between the groups and between sexes as far as the body weight gains are concerned. The males showed smaller mean gains than the females, but reacted more distinctly to the stimulating action of the studied antibiotics.

Animal Feed↗